9FLZ

Alcohol dehydrogenase

9FLZ の概要

• エントリーDOI: 10.2210/pdb9flz/pdb
• EMDBエントリー: 50545
• 分子名称: alcohol dehydrogenase, ZINC ION (3 entities in total)
• 機能のキーワード: alcohol dehydrogenase, tetramer, oxidoreductase
• 由来する生物種: Paracoccus denitrificans
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 155308.21

構造登録者

Lamers, M.H.,Schada von Borzyskowski, L.,Ren, M. (登録日: 2024-06-05, 公開日: 2025-06-11, 最終更新日: 2026-02-04)

主引用文献

Ren, M.,Li, D.,Addison, H.,Noteborn, W.E.M.,Andeweg, E.H.,Glatter, T.,de Winde, J.H.,Rebelein, J.G.,Lamers, M.H.,Schada von Borzyskowski, L.
NAD-dependent dehydrogenases enable efficient growth of Paracoccus denitrificans on the PET monomer ethylene glycol.
Nat Commun, 16:5845-5845, 2025

PubMed Abstract: Ethylene glycol is a monomer of the plastic polyethylene terephthalate (PET) and an environmental pollutant of increasing concern. Although it is generally accepted that bacteria use ethylene glycol as growth substrate, not all involved enzymes are well understood. Here, we show that Paracoccus denitrificans assimilates ethylene glycol solely via NAD-dependent alcohol and aldehyde dehydrogenases. Using comparative proteomics, we identify a gene cluster that is strongly expressed in the presence of ethylene glycol. We report the functional and structural characterization of EtgB and EtgA, key enzymes encoded by this etg gene cluster. We furthermore show that the transcriptional activator EtgR controls expression of the gene cluster. Adaptive laboratory evolution on ethylene glycol results in faster growth, enabled by increased production of EtgB and EtgA. Bioinformatic analysis reveals that the etg gene cluster is widely distributed among bacteria, suggesting a common role of NAD-dependent dehydrogenases in microbial ethylene glycol assimilation.

PubMed: 40592898
DOI: 10.1038/s41467-025-61056-x

実験手法

ELECTRON MICROSCOPY (3 Å)